Dissertation / PhD Thesis/Book PreJuSER-26980

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Untersuchungen zu einem neuen Isopentenyldiphosphat-Biosyntheseweg in Escherichia coli und Zymomonas mobilis : Identifizierung und Charakterisierung beteiligter Gene



2000
Forschungszentrum Jülich GmbH Zentralbibliothek, Verlag Jülich

Jülich : Forschungszentrum Jülich GmbH Zentralbibliothek, Verlag, Berichte des Forschungszentrums Jülich 3799, V, 111 p. () = Düsseldorf, Univ., Diss., 2000

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Report No.: Juel-3799

Abstract: In the last few years, evidence has emerged that in bacteria a novel biosynthetic pathway to isopentenyl diphosphate exists. In this pathway isopentenyl diphosphate is formed from pyruvate and glyceraldehyde 3-phosphate. In the first reaction step these C4 compounds are combined to 1-deoxyxylulose 5-phosphate synthase was identified in $\textit{E. coli}$ by searching for transketolase-homologous genes. The corresponding gene product was purified and was shown by NMR analysis to catalyze in a thiamin diphosphate (TPP) and Mg$^{2}$ dependent reaction the synthesis of 1-deoxyxylulose 5-phosphate. Phylogenetic investigation revealed that the 1-deoxyxylulose 5-phosphate synthase belongs to a new family of TPP dependent enzymes. The $\textit{dxs}$ gene is located at 9 min on the $\textit{E. coli}$ chromosome and is organized in one operon with a putative aldoketo-reductase gene. The disruption of this $\textit{E. coli}$ gene yielded no phenotype which indicates that the gene is not involved in the novel pathway. The gene encoding the second enzyme of the pathway, the 1-deoxyxylulose 5-phosphate reductoisomerase, was isolated from $\textit{Z. mobilis}$. The 1-deoxyxylulose 4-phosphate reductoisomerase catalyzes the NADPH and Mn$^{2}$ dependent rearrangement and subsequent reduction of 1-deoxyxylulose 5-phosphate to 2C-methylerythritol 4-phosphate. The enzyme activity is competitively inhibited by the antibiotic fosmidomycin with a K$_{i}$ of 0,6 $\mu$M. By using a $\textit{E. coli}$ strain engineered to produce the isoprenoide zeaxanthin the gene encoding IPP-isomerase, but no further genes of the novel pathway could be isolated from an $\textit{E. coli}$ expression gene library.


Note: Record converted from VDB: 12.11.2012
Note: Düsseldorf, Univ., Diss., 2000

Contributing Institute(s):
  1. Institut für Biotechnologie (IBT)
Research Program(s):
  1. Mikrobiologische Grundlagen der Gewinnung von Proteinen (41.35.1)

Appears in the scientific report 2000
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 Record created 2012-11-13, last modified 2020-06-10